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HighlightsPolycystic kidney disease-2-like 1 (PKD2L1) is a member of the polycystin protein family consisting of PKD2 (polycystin-2), PKD2L1, and PKD2L2. PKD2L1 was first identified as a gene homologous to PKD2. Human PKD2L1 shows 50% amino acid sequence identity and 71% similarity with PKD2. PKD2L1 contains a putative Ca2+ binding EF hand motif and a predicted coiled-coil domain in its C-terminal cytoplasmic tail.
| Basic Information of PKD2L1 | |
| Protein Name | Polycystic kidney disease 2-like 1 protein |
| Gene Name | PKD2L1 |
| Aliases | Polycystin-2 homolog, Polycystin-2L1, Polycystin-L, Polycystin-L1 |
| Organism | Homo sapiens (Human) |
| UniProt ID | Q9P0L9 |
| Transmembrane Times | 6 |
| Length (aa) | 805 |
| Sequence | MNAVGSPEGQELQKLGSGAWDNPAYSGPPSPHGTLRVCTISSTGPLQPQPKKPEDEPQETAYRTQVSSCCLHICQGIRGLWGTTLTENTAENRELYIKTTLRELLVYIVFLVDICLLTYGMTSSSAYYYTKVMSELFLHTPSDTGVSFQAISSMADFWDFAQGPLLDSLYWTKWYNNQSLGHGSHSFIYYENMLLGVPRLRQLKVRNDSCVVHEDFREDILSCYDVYSPDKEEQLPFGPFNGTAWTYHSQDELGGFSHWGRLTSYSGGGYYLDLPGSRQGSAEALRALQEGLWLDRGTRVVFIDFSVYNANINLFCVLRLVVEFPATGGAIPSWQIRTVKLIRYVSNWDFFIVGCEVIFCVFIFYYVVEEILELHIHRLRYLSSIWNILDLVVILLSIVAVGFHIFRTLEVNRLMGKLLQQPNTYADFEFLAFWQTQYNNMNAVNLFFAWIKIFKYISFNKTMTQLSSTLARCAKDILGFAVMFFIVFFAYAQLGYLLFGTQVENFSTFIKCIFTQFRIILGDFDYNAIDNANRILGPAYFVTYVFFVFFVLLNMFLAIINDTYSEVKEELAGQKDELQLSDLLKQGYNKTLLRLRLRKERVSDVQKVLQGGEQEIQFEDFTNTLRELGHAEHEITELTATFTKFDRDGNRILDEKEQEKMRQDLEEERVALNTEIEKLGRSIVSSPQGKSGPEAARAGGWVSGEEFYMLTRRVLQLETVLEGVVSQIDAVGSKLKMLERKGWLAPSPGVKEQAIWKHPQPAPAVTPDPWGVQGGQESEVPYKREEEALEERRLSRGEIPTLQRS |
PKD2L1 is also believed to be a nonselective cation channel that can be regulated by voltage, protons, and calcium. It has been revealed that PKD2L1 is involved in the sour sensation and other pH-dependent processes. PKD2L1 has been shown to express in a discrete population of neurons surrounding the central canal of the spinal cord and may function to monitor the pH of the cerebrospinal fluid. In gustatory cells, pore-forming subunit of a channel formed by PKD1L2 and PKD1L3 contributes to sour taste perception.
Fig.1 Several models of sour taste detection. (Ishimaru, 2009)
In this study, the authors observe the activity of PKD2L1 channel increased by the downstream cascades of β2AR and find the clustered phosphorylation sites, Ser-682, Ser-685, and Ser-686 that are significant in the channel regulation by phosphorylation.
This study suggests that PKD2L1 may itself sense acids and defines off-response properties in the absence of PKD1L3.
This study identifies C1 as the first PKD2L1 domain essential for both PKD2L1 trimerization and channel function, and suggests that PKD2L1 and PKD2L1/PKD1L3 channels share the PKD2L1 trimerization process.
This study reveals the pore domain dilation is coupled to conformational changes of voltage-sensing domains (VSDs) via a series of π-π interactions, which suggests a potential PKD2L1 gating mechanism.
This report suggests that the N533 residue in the outer pore loop region of PKD2L1 plays an essential role in the voltage-dependent channel inactivation.
We provide custom membrane protein preparation services for worldwide customers. Leveraging by our advanced Magic™ membrane protein production platform, we are able to present target membrane protein in multiple active formats. Our professional scientists are happy to help you find an ideal method and make your project a success. Besides, aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-PKD2L1 antibody development services.
Creative Biolabs provides high-quality membrane protein preparation service to facilitate the development of worldwide customer’s research. During the past years, we have successfully established a powerful Magic™ membrane protein platform which enables us to provide a series of membrane protein preparation services. For more detailed information, please feel free to contact us.
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